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Cooperation between the intrinsically disordered and ordered regions of SPT6 regulates nucleosome and pol II ctd binding, and nucleosome assembly

Analyse Cooperation between the intrinsically disordered and ordered regions of SPT6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7O3D
Type
protein
Length
709 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription elongation factor SPT6
UniProt
P23615
Pockets
12 · best druggability 0.72

Structure

electron microscopy · 1 distinct chain · 50% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription elongation factor SPT6protein70950% helix, 9% strandP23615

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15370.720.8145empty
25460.700.7954empty
35060.690.7950empty
4680.670.9422empty
52200.570.7927empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7O3D · Cooperation between the intrinsically disordered and ordered regions of Spt6 regulates… · the same entry in another collection · chain A against A, TM-score 1.00
  • P23615 · AlphaFold monomer V2.0 prediction for transcription elongation factor SPT6 (P23615) · a predicted model of the same protein · chain A against A, TM-score 0.97

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